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Protein

Probetacellulin

Gene

Btc

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Growth factor that binds to EGFR, ERBB4 and other EGF receptor family members. Potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells.1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Growth factor, Mitogen

Enzyme and pathway databases

ReactomeiR-MMU-1227986. Signaling by ERBB2.
R-MMU-1236394. Signaling by ERBB4.
R-MMU-1250196. SHC1 events in ERBB2 signaling.
R-MMU-1250342. PI3K events in ERBB4 signaling.
R-MMU-1250347. SHC1 events in ERBB4 signaling.
R-MMU-1257604. PIP3 activates AKT signaling.
R-MMU-1963640. GRB2 events in ERBB2 signaling.
R-MMU-1963642. PI3K events in ERBB2 signaling.
R-MMU-5673001. RAF/MAP kinase cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
Probetacellulin
Cleaved into the following chain:
Betacellulin
Short name:
BTC
Gene namesi
Name:Btc
Synonyms:Bcn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:99439. Btc.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini32 – 11887ExtracellularSequence analysisAdd
BLAST
Transmembranei119 – 13921HelicalSequence analysisAdd
BLAST
Topological domaini140 – 17738CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • extracellular space Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: MGI
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 31311 PublicationAdd
BLAST
Chaini32 – 177146ProbetacellulinPRO_0000300686Add
BLAST
Chaini32 – 11180BetacellulinPRO_0000007492Add
BLAST
Propeptidei112 – 17766Removed in mature formPRO_0000007493Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi34 – 341N-linked (GlcNAc...)Sequence analysis
Glycosylationi42 – 421N-linked (GlcNAc...)Sequence analysis
Glycosylationi52 – 521N-linked (GlcNAc...)Sequence analysis
Disulfide bondi69 ↔ 82PROSITE-ProRule annotation
Disulfide bondi77 ↔ 93PROSITE-ProRule annotation
Disulfide bondi95 ↔ 104PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ05928.
PRIDEiQ05928.

Miscellaneous databases

PMAP-CutDBQ05928.

Expressioni

Tissue specificityi

Found in several mouse tissues including kidney, uterus and liver, as well as in beta tumor cell line and MCF-7 cells. It is not detected in the brain.

Gene expression databases

BgeeiQ05928.
ExpressionAtlasiQ05928. baseline and differential.
GenevisibleiQ05928. MM.

Interactioni

Subunit structurei

Monomer. Interacts with EGFR and ERBB4.

Protein-protein interaction databases

BioGridi198395. 2 interactions.
STRINGi10090.ENSMUSP00000112765.

Structurei

3D structure databases

ProteinModelPortaliQ05928.
SMRiQ05928. Positions 63-111.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini65 – 10541EGF-likePROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi146 – 1538Arg/Lys-rich (basic)

Sequence similaritiesi

Contains 1 EGF-like domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IWUI. Eukaryota.
ENOG41126JP. LUCA.
HOGENOMiHOG000237352.
HOVERGENiHBG004905.
InParanoidiQ05928.
KOiK09783.
OMAiIGARCER.
OrthoDBiEOG7VQJGP.
PhylomeDBiQ05928.
TreeFamiTF332938.

Family and domain databases

InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR015497. EGF_rcpt_ligand.
[Graphical view]
PANTHERiPTHR10740. PTHR10740. 1 hit.
PfamiPF00008. EGF. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q05928-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPTAPGSSV SSLPLLLVLA LGLAILHCVV ADGNTTRTPE TNGSLCGAPG
60 70 80 90 100
ENCTGTTPRQ KVKTHFSRCP KQYKHYCIHG RCRFVVDEQT PSCICEKGYF
110 120 130 140 150
GARCERVDLF YLQQDRGQIL VVCLIVVMVV FIILVIGVCT CCHPLRKHRK
160 170
KKKEEKMETL DKDKTPISED IQETNIA
Length:177
Mass (Da):19,664
Last modified:February 1, 1994 - v1
Checksum:i066BB34F0E13F82B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08394 mRNA. Translation: AAA40511.1.
AK076272 mRNA. Translation: BAC36281.1.
CCDSiCCDS19422.1.
PIRiA37408.
RefSeqiNP_031594.1. NM_007568.5.
UniGeneiMm.2024.

Genome annotation databases

EnsembliENSMUST00000121044; ENSMUSP00000112765; ENSMUSG00000082361.
GeneIDi12223.
KEGGimmu:12223.
UCSCiuc008ybv.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08394 mRNA. Translation: AAA40511.1.
AK076272 mRNA. Translation: BAC36281.1.
CCDSiCCDS19422.1.
PIRiA37408.
RefSeqiNP_031594.1. NM_007568.5.
UniGeneiMm.2024.

3D structure databases

ProteinModelPortaliQ05928.
SMRiQ05928. Positions 63-111.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198395. 2 interactions.
STRINGi10090.ENSMUSP00000112765.

Proteomic databases

PaxDbiQ05928.
PRIDEiQ05928.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000121044; ENSMUSP00000112765; ENSMUSG00000082361.
GeneIDi12223.
KEGGimmu:12223.
UCSCiuc008ybv.2. mouse.

Organism-specific databases

CTDi685.
MGIiMGI:99439. Btc.

Phylogenomic databases

eggNOGiENOG410IWUI. Eukaryota.
ENOG41126JP. LUCA.
HOGENOMiHOG000237352.
HOVERGENiHBG004905.
InParanoidiQ05928.
KOiK09783.
OMAiIGARCER.
OrthoDBiEOG7VQJGP.
PhylomeDBiQ05928.
TreeFamiTF332938.

Enzyme and pathway databases

ReactomeiR-MMU-1227986. Signaling by ERBB2.
R-MMU-1236394. Signaling by ERBB4.
R-MMU-1250196. SHC1 events in ERBB2 signaling.
R-MMU-1250342. PI3K events in ERBB4 signaling.
R-MMU-1250347. SHC1 events in ERBB4 signaling.
R-MMU-1257604. PIP3 activates AKT signaling.
R-MMU-1963640. GRB2 events in ERBB2 signaling.
R-MMU-1963642. PI3K events in ERBB2 signaling.
R-MMU-5673001. RAF/MAP kinase cascade.

Miscellaneous databases

NextBioi280627.
PMAP-CutDBQ05928.
PROiQ05928.
SOURCEiSearch...

Gene expression databases

BgeeiQ05928.
ExpressionAtlasiQ05928. baseline and differential.
GenevisibleiQ05928. MM.

Family and domain databases

InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR015497. EGF_rcpt_ligand.
[Graphical view]
PANTHERiPTHR10740. PTHR10740. 1 hit.
PfamiPF00008. EGF. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Betacellulin: a mitogen from pancreatic beta cell tumors."
    Shing Y., Christofori G., Hanahan D., Ono Y., Sasada R., Igarashi K., Folkman J.
    Science 259:1604-1607(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 32-54; 64-71 AND 75-111.
    Tissue: Pancreas.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Skin.
  3. "Betacellulin-induced beta cell proliferation and regeneration is mediated by activation of ErbB-1 and ErbB-2 receptors."
    Oh Y.S., Shin S., Lee Y.J., Kim E.H., Jun H.S.
    PLoS ONE 6:E23894-E23894(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiBTC_MOUSE
AccessioniPrimary (citable) accession number: Q05928
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: May 11, 2016
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.